Search by BoMiProt ID - Bomi82


Primary Information

BoMiProt ID Bomi82
Protein Name Sorting nexin-17
Organism Bos taurus
Uniprot IDQ5EA77
Milk FractionExosome
Ref Sequence ID NP_001015638.1
Aminoacid Length 470
Molecular Weight 52825
FASTA Sequence Download
Gene Name SNX17
Gene ID 529972
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Protein Function involved in protein sorting, cellular trafficking and endocytosis; potential for membrane association; SNX17 can interact with P-selectin;
Biochemical Properties hydrophilic molecules;presence of phospholipid binding motif that binds to various phophatidylinositol phospahtes; presence of various protein-protein interaction motifs, membrane targeting sequences and G protein regulatory sequences; SNX1 is both membrane asscoiated and cytosolic-exist as tetramer as a large protein complex
PTMs serine/threonine phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions 400-426
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs SNX9 tyrosine phosphorylation by ACK results to switch in protein-protein interaction partners
Linking IDs
Bibliography 1. Lin, Q., Lo, C. G., Cerione, R. A., & Yang, W. (2002). The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation. The Journal of Biological Chemistry, 277(12), 10134–10138. https://doi.org/10.1074/jbc.M110329200.
2. Shaw, R. J., Henry, M., Solomon, F., & Jacks, T. (1998). RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Molecular Biology of the Cell, 9(2), 403–419. https://doi.org/10.1091/mbc.9.2.403.
3. Lamb, J. R., Tugendreich, S., & Hieter, P. (1995). Tetratrico peptide repeat interactions: to TPR or not to TPR? Trends in Biochemical Sciences, 20(7), 257–259. https://doi.org/10.1016/s0968-0004(00)89037-4.
4. Kanai, F., Liu, H., Field, S. J., Akbary, H., Matsuo, T., Brown, G. E., … Yaffe, M. B. (2001). The PX domains of p47phox and p40phox bind to lipid products of PI(3)K. Nature Cell Biology, 3(7), 675–678. https://doi.org/10.1038/35083070.
5. Xu, Y., Seet, L. F., Hanson, B., & Hong, W. (2001, December 15). The Phox homology (PX) domain, a new player in phosphoinositide signalling. Biochemical Journal, Vol. 360, pp. 513–530. https://doi.org/10.1042/0264-6021:3600513.